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Protein let-653 (Lethal protein 653)

 LE653_CAEEL             Reviewed;         812 AA.
Q27394; G5ECH8; Q5WRN8;
18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 2.
30-AUG-2017, entry version 121.
RecName: Full=Protein let-653 {ECO:0000305};
AltName: Full=Lethal protein 653 {ECO:0000312|WormBase:C29E6.1a};
Flags: Precursor;
Name=let-653 {ECO:0000312|WormBase:C29E6.1a};
ORFNames=C29E6.1 {ECO:0000312|WormBase:C29E6.1a};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|EMBL:CAA62505.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM C), AND FUNCTION.
STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA62505.1};
PubMed=7476875; DOI=10.1007/BF02191712;
Jones S.J.M., Baillie D.L.;
"Characterization of the let-653 gene in Caenorhabditis elegans.";
Mol. Gen. Genet. 248:719-726(1995).
[2] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, DOMAIN, PROTEOLYTIC CLEAVAGE, AND DISRUPTION PHENOTYPE.
PubMed=27482894; DOI=10.1371/journal.pgen.1006205;
Gill H.K., Cohen J.D., Ayala-Figueroa J., Forman-Rubinsky R.,
Poggioli C., Bickard K., Parry J.M., Pu P., Hall D.H., Sundaram M.V.;
"Integrity of narrow epithelial tubes in the C. elegans excretory
system requires a transient luminal matrix.";
PLoS Genet. 12:E1006205-E1006205(2016).
-!- FUNCTION: Required for epithelial tube development and shaping
(PubMed:27482894). Involved in the morphogenesis and function of
the three unicellular tubes of the excretory system, the canal
cell, the duct cell and the pore cell (PubMed:7476875,
PubMed:27482894). Also plays a role in cuticle development, alae
formation and shaping of the vulval lumen (PubMed:27482894).
Required for larval development (PubMed:7476875, PubMed:27482894).
{ECO:0000269|PubMed:27482894, ECO:0000269|PubMed:7476875}.
-!- SUBCELLULAR LOCATION: Isoform b: Apical cell membrane
{ECO:0000269|PubMed:27482894}; Peripheral membrane protein
{ECO:0000269|PubMed:27482894}; Lumenal side
{ECO:0000269|PubMed:27482894}. Secreted, extracellular space
{ECO:0000269|PubMed:27482894}. Secreted
{ECO:0000269|PubMed:27482894}. Note=Localizes to fibrils in the
vulval luminal space. {ECO:0000269|PubMed:27482894}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=a {ECO:0000312|WormBase:C29E6.1a};
IsoId=Q27394-1; Sequence=Displayed;
Name=b {ECO:0000312|WormBase:C29E6.1b};
IsoId=Q27394-2; Sequence=VSP_058741;
Name=c {ECO:0000312|WormBase:C29E6.1c};
IsoId=Q27394-3; Sequence=VSP_058742;
-!- TISSUE SPECIFICITY: Isoform b: Expressed in external cuticle-
producing epithelial cells including the epidermis, vulva, rectum,
excretory duct and excretory pore. {ECO:0000269|PubMed:27482894}.
-!- DEVELOPMENTAL STAGE: Isoform b: Secreted in the region between the
embryo and inner layer of the eggshell. Expressed in excretory
canal cells of embryos and at the 1.5-fold stage of embryonic
development accumulates in the lumen of the excretory duct and
pore. Expression ceases in the lumen of the excretory duct and
pore prior to cuticle secretion. Thereafter expressed transiently
in the lumen of the excretory duct and pore in the latter phase of
each subsequent larval developmental stage. During the molt phase
of larval development, accumulates in the space in between the new
and old cuticles. During the L4 stage of larval development,
accumulates in the vulval lumen. {ECO:0000269|PubMed:27482894}.
-!- DOMAIN: Isoform b: The ZP domain is required for localization at
the apical cell membrane, secretion and excretory tube and vulval
lumen expansion. {ECO:0000269|PubMed:27482894}.
-!- PTM: Isoform b: Cleaved at the C-terminal domain.
{ECO:0000269|PubMed:27482894}.
-!- DISRUPTION PHENOTYPE: Lethal at the larval stage of development.
Defects in the development of the excretory system during
embryogenesis and the early stages of larval development. Dilated
lumens of both the excretory canal cell and excretory duct which
become apparent between the early and mid 3-fold stages of
embryogenesis and increases in severity as development progresses.
Lumen dialation may be as a result of fluid accumulation due to
blockage of the lumen. At around the time of hatching, the
autocellular junction, which usually seals the excretory pore
tube, is absent. Detached excretory duct and pore cells, which
usually connects the excretory canal cell to the outside
environment for excretion. Irregular morphology of the epidermis
and vulva in larvae at the L1 stage of larval development.
{ECO:0000269|PubMed:27482894}.
-----------------------------------------------------------------------
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EMBL; X91045; CAA62505.1; -; Genomic_DNA.
EMBL; BX284604; CAA96602.2; -; Genomic_DNA.
EMBL; BX284604; CAH60755.1; -; Genomic_DNA.
EMBL; BX284604; CCD31038.1; -; Genomic_DNA.
PIR; T19551; T19551.
RefSeq; NP_001021336.2; NM_001026165.4. [Q27394-1]
RefSeq; NP_001021337.1; NM_001026166.3. [Q27394-2]
RefSeq; NP_001255594.1; NM_001268665.1. [Q27394-3]
UniGene; Cel.17069; -.
ProteinModelPortal; Q27394; -.
SMR; Q27394; -.
STRING; 6239.C29E6.1a.2; -.
EPD; Q27394; -.
PaxDb; Q27394; -.
EnsemblMetazoa; C29E6.1a.1; C29E6.1a.1; WBGene00002827. [Q27394-1]
EnsemblMetazoa; C29E6.1a.2; C29E6.1a.2; WBGene00002827. [Q27394-1]
EnsemblMetazoa; C29E6.1b.1; C29E6.1b.1; WBGene00002827. [Q27394-2]
EnsemblMetazoa; C29E6.1b.2; C29E6.1b.2; WBGene00002827. [Q27394-2]
EnsemblMetazoa; C29E6.1c.1; C29E6.1c.1; WBGene00002827. [Q27394-3]
EnsemblMetazoa; C29E6.1c.2; C29E6.1c.2; WBGene00002827. [Q27394-3]
GeneID; 178120; -.
KEGG; cel:CELE_C29E6.1; -.
UCSC; C29E6.1b.1; c. elegans. [Q27394-1]
CTD; 178120; -.
WormBase; C29E6.1a; CE40548; WBGene00002827; let-653. [Q27394-1]
WormBase; C29E6.1b; CE37323; WBGene00002827; let-653. [Q27394-2]
WormBase; C29E6.1c; CE05332; WBGene00002827; let-653. [Q27394-3]
eggNOG; ENOG410JAZ6; Eukaryota.
eggNOG; ENOG410YFJE; LUCA.
HOGENOM; HOG000017921; -.
InParanoid; Q27394; -.
OMA; YENNCYN; -.
OrthoDB; EOG091G03TV; -.
PRO; PR:Q27394; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00002827; -.
GO; GO:0098592; C:cytoplasmic side of apical plasma membrane; IDA:UniProtKB.
GO; GO:0098591; C:external side of apical plasma membrane; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0099512; C:supramolecular fiber; IDA:UniProtKB.
GO; GO:0042302; F:structural constituent of cuticle; IMP:UniProtKB.
GO; GO:0009653; P:anatomical structure morphogenesis; IMP:UniProtKB.
GO; GO:0035017; P:cuticle pattern formation; IMP:UniProtKB.
GO; GO:0048613; P:embryonic ectodermal digestive tract morphogenesis; IMP:UniProtKB.
GO; GO:0002064; P:epithelial cell development; IMP:WormBase.
GO; GO:1903133; P:negative regulation of tube lumen cavitation; IMP:UniProtKB.
GO; GO:1905278; P:positive regulation of epithelial tube formation; IMP:UniProtKB.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:UniProtKB.
GO; GO:0061063; P:positive regulation of nematode larval development; IMP:UniProtKB.
GO; GO:0040026; P:positive regulation of vulval development; IMP:UniProtKB.
GO; GO:0035150; P:regulation of tube size; IMP:WormBase.
InterPro; IPR003609; Pan_app.
InterPro; IPR001507; ZP_dom.
Pfam; PF00024; PAN_1; 1.
SMART; SM00473; PAN_AP; 2.
SMART; SM00241; ZP; 1.
PROSITE; PS50948; PAN; 2.
PROSITE; PS51034; ZP_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Developmental protein; Disulfide bond; Glycoprotein; Membrane;
Reference proteome; Secreted; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 812 Protein let-653. {ECO:0000305}.
/FTId=PRO_5004203492.
DOMAIN 26 116 Apple 1. {ECO:0000255|PROSITE-
ProRule:PRU00315}.
DOMAIN 123 209 Apple 2. {ECO:0000255|PROSITE-
ProRule:PRU00315}.
DOMAIN 221 725 ZP. {ECO:0000255|PROSITE-
ProRule:PRU00375}.
COMPBIAS 367 576 Thr-rich. {ECO:0000255|PROSITE-
ProRule:PRU00017}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 211 211 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 771 771 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 26 116 {ECO:0000255|PROSITE-ProRule:PRU00315}.
DISULFID 53 88 {ECO:0000255|PROSITE-ProRule:PRU00315}.
DISULFID 57 72 {ECO:0000255|PROSITE-ProRule:PRU00315}.
DISULFID 123 209 {ECO:0000255|PROSITE-ProRule:PRU00315}.
DISULFID 154 178 {ECO:0000255|PROSITE-ProRule:PRU00315}.
DISULFID 158 166 {ECO:0000255|PROSITE-ProRule:PRU00315}.
VAR_SEQ 334 493 RNKAMEASAHALFELLSKTGDDEALQNTFPLPLTTTTEVIR
QVTTTTKKPSTTTSTKKLTTTTTTTPKPSQKPTTTTTKSPV
VITTTTKTSPKPTTSPSTTTSTTTSTTIPPSTTTRKPANPR
RSTIMSATSKVAIIVGKDSSFARARLFTTKHPSTQKI ->
S (in isoform b). {ECO:0000305}.
/FTId=VSP_058741.
VAR_SEQ 374 493 RQVTTTTKKPSTTTSTKKLTTTTTTTPKPSQKPTTTTTKSP
VVITTTTKTSPKPTTSPSTTTSTTTSTTIPPSTTTRKPANP
RRSTIMSATSKVAIIVGKDSSFARARLFTTKHPSTQKI ->
S (in isoform c). {ECO:0000305}.
/FTId=VSP_058742.
SEQUENCE 812 AA; 89480 MW; 0E491EC768A43C60 CRC64;
MRHPLISLLL LIAFYSTSSE AFVPKCNSFY VRWPRVRLNF KAVAEARLSL KGCQSACSLG
EDPVSPGKQL ECAAVNHQAS PDGFSHLCAV FQPHQLQNVD GYVEADDRFT FYWKYCLPST
RKCSGEYAFT YLSDRYMDQK SVIKWTTKAN LEECLSDCLD EKSFECRSIS FNRTDGGCHM
SKDSQISRPE AIRLNNNPNY RIDYYENNCY NLSESFTFKH ECRDNGISVS VKSRLPYTGA
IYGLYDFFTC RTEPKEATEF DHFFPYQTVS KNCSDSIKYK GNEMVLEVVL STDGIEPLYF
ITPEDLTYQA KCPISGVKAK DPANTKSSAH LDNRNKAMEA SAHALFELLS KTGDDEALQN
TFPLPLTTTT EVIRQVTTTT KKPSTTTSTK KLTTTTTTTP KPSQKPTTTT TKSPVVITTT
TKTSPKPTTS PSTTTSTTTS TTIPPSTTTR KPANPRRSTI MSATSKVAII VGKDSSFARA
RLFTTKHPST QKIDVPTTTV QTSTTVPTTP SKTTATTTTT PKPTTTETAT TSSSTTTVTT
QKPTTVTSTT TLPSTTASTT TKTTTSTPTS PQTTTTHVGA PASSVASVAH DGSTLAGKPK
VPVIFDIFHN GQPVEAVVVG TKISLSFRPH YPIPPEYVDV RGCQVEPIDP KYEWEHEPLF
IIRDGCPADG VGLVCPPTHS EFGAKVSVEA FRYQTTGQVQ YSCLVRICPF APCPKNTCDD
VEGCDSSYMH RYRRELSLED IKKALEANPE LASQFGISPS AFARNPSKSK NFTSVVEEQQ
RIALGGDYLV RRRLIVVNSE DQLRYYVRTG NI


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